Identification of novel broad-spectrum antiviral drugs targeting the N-terminal domain of the FIPV nucleocapsid protein.

Identification of novel broad-spectrum antiviral drugs targeting the N-terminal domain of the FIPV nucleocapsid protein.

Publication date: Nov 01, 2024

Coronaviruses pose serious threats to human and animal health worldwide, of which their structural nucleocapsid (N) proteins play multiple key roles in viral replication. However, the structures of animal coronavirus N proteins are poorly understood, posing challenges for research on their functions and pathogenic mechanisms as well as the development of N protein-based antiviral drugs. Therefore, N proteins must be further explored as potential antiviral targets. We determined the structure of the NNTD of feline infectious peritonitis virus (FIPV) and identified 3,6-dihydroxyflavone (3,6- DHF) as an effective N protein inhibitor. 3,6-DHF successfully inhibited FIPV replication in CRFK cells, showing broad-spectrum activity and effectiveness against drugresistant strains. Our study provides important insights for developing novel broadspectrum anti-coronavirus drugs and treating infections caused by drug-resistant mutant strains.

Concepts Keywords
Coronaviruses Animals
Dihydroxyflavone Antiviral Agents
Effective Antiviral Agents
Mutant Antivirals
Pathogenic Broad-spectrum
Cats
Cell Line
Coronavirus
Coronavirus Nucleocapsid Proteins
Coronavirus Nucleocapsid Proteins
Coronavirus, Feline
Drug Resistance, Viral
Nucleocapsid protein
Nucleocapsid Proteins
Nucleocapsid Proteins
Protein Domains
Resistant
Virus Replication

Semantics

Type Source Name
pathway KEGG Viral replication
disease IDO protein
disease IDO replication
disease MESH infections
disease IDO cell

Original Article

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